ID MSB1_YEAST Reviewed; 1137 AA. AC P21339; D6W2P4; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 27-MAR-2024, entry version 169. DE RecName: Full=Morphogenesis-related protein MSB1; DE AltName: Full=Multicopy suppressor of bud emergence 1; GN Name=MSB1; OrderedLocusNames=YOR188W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1996092; DOI=10.1128/mcb.11.3.1295-1305.1991; RA Bender A., Pringle J.R.; RT "Use of a screen for synthetic lethal and multicopy suppressee mutants to RT identify two new genes involved in morphogenesis in Saccharomyces RT cerevisiae."; RL Mol. Cell. Biol. 11:1295-1305(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169874; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538 AND SER-816, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538 AND SER-776, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: May play a role in polarity establishment and bud formation. CC The MSB1 gene may be functionally redundant. CC -!- INTERACTION: CC P21339; P40073: SHO1; NbExp=2; IntAct=EBI-11322, EBI-18140; CC -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M37767; AAA34797.1; -; Genomic_DNA. DR EMBL; Z75096; CAA99397.1; -; Genomic_DNA. DR EMBL; BK006948; DAA10960.1; -; Genomic_DNA. DR PIR; S13759; S13759. DR RefSeq; NP_014831.3; NM_001183607.3. DR AlphaFoldDB; P21339; -. DR BioGRID; 34583; 83. DR DIP; DIP-2687N; -. DR IntAct; P21339; 5. DR MINT; P21339; -. DR STRING; 4932.YOR188W; -. DR iPTMnet; P21339; -. DR MaxQB; P21339; -. DR PaxDb; 4932-YOR188W; -. DR PeptideAtlas; P21339; -. DR EnsemblFungi; YOR188W_mRNA; YOR188W; YOR188W. DR GeneID; 854360; -. DR KEGG; sce:YOR188W; -. DR AGR; SGD:S000005714; -. DR SGD; S000005714; MSB1. DR VEuPathDB; FungiDB:YOR188W; -. DR eggNOG; ENOG502QUEY; Eukaryota. DR HOGENOM; CLU_004952_0_0_1; -. DR InParanoid; P21339; -. DR OMA; LETHLEM; -. DR OrthoDB; 2727882at2759; -. DR BioCyc; YEAST:G3O-33698-MONOMER; -. DR BioGRID-ORCS; 854360; 0 hits in 10 CRISPR screens. DR PRO; PR:P21339; -. DR Proteomes; UP000002311; Chromosome XV. DR RNAct; P21339; Protein. DR GO; GO:0005935; C:cellular bud neck; HDA:SGD. DR GO; GO:0005934; C:cellular bud tip; HDA:SGD. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0005886; C:plasma membrane; HDA:SGD. DR GO; GO:0030010; P:establishment of cell polarity; IGI:SGD. DR CDD; cd04401; RhoGAP_fMSB1; 1. DR InterPro; IPR037508; Msb1/Mug8. DR InterPro; IPR012965; Msb1/Mug8_dom. DR PANTHER; PTHR28093; MORPHOGENESIS-RELATED PROTEIN MSB1; 1. DR PANTHER; PTHR28093:SF1; MORPHOGENESIS-RELATED PROTEIN MSB1; 1. DR Pfam; PF08101; Msb1-Mug8_dom; 1. PE 1: Evidence at protein level; KW Phosphoprotein; Reference proteome. FT CHAIN 1..1137 FT /note="Morphogenesis-related protein MSB1" FT /id="PRO_0000096588" FT REGION 1..59 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 483..520 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 577..620 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 736..799 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 814..871 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 25..46 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 577..595 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 596..620 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 747..767 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 768..799 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 538 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MOD_RES 776 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 816 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950" SQ SEQUENCE 1137 AA; 129971 MW; 59CDD6E0F1E43F8A CRC64; MNDMAKPLPT PPTAEIRKSR SNSPKKAQKT NLSPNKNQNN EKNVPRSNGR TKNEHNSMDD EEFEFFHQFS REKVKGVIHV ITAELKEKGP DVEFLMIPFR PEQTNDKLLT LLNQLFPLGN GQPVNEKKQL RIVSKADVWT LFQCLKYIWC RLPNSEIIGW KSYLEFKFRE EDKKFPRKSF LEIMPQCLAS PNHASIVYDF FDLIISISSN SRVNKMSARK ISKMCAIWAF SKQIPNSDIQ DYDFESAAMK SFAPNNSIQD GLDQWIPASD AMFHLLLAFL RSFVPQDLES AKLPRTLKSL LFNNQYPPRK STAYTSETIL TIPLVTLKTD VFSRKPWQLL ERCNDLLDFS DHDAFEARED YALLKSLFRK KNTVEGISRK MSQESRRLMK AMSTKHSTFQ PGWAPRECIE NISHLKECIE VKRLDIDDYF IWTWLSSLSF EQTSEKKKIF GRSIILEFEF DGFKKWVVFQ ECDITLDYNK KGQLKKKTSA QSPTTEKELP PDDFELEDPP LSKSPTLSQT YKKFQAEVPQ QSTVRRDSAP DNQGIYHTVI SKNALTKNKH NVNLHSFEHK ISKWNPLNNL RKKSGSNSSS SSFEEKSKDA PIREEYHTNK NHKSKKEERV LSQFSTLNPD EYQLPVIETG SSNFKIEIPE LMYEHDDDDS DKLKNSQKRA TDSAIEELNG MVEEMMINEP DDVKISITEA ETFESLTKFD QYKPSNITDD DLQSSHSSAV HSLKLSTNTN DSCADSSKYT ADRKLAEPRK ISEESKVNDD SSSYYSPNIN NLPASRMPSQ PTYSNSDSKK AFTNESRLNV LQGAVSPSQQ VTPKPYKNAP GDCVSPVQQK YYQNDRRNEM SPASAPVPPS AYSPARSPQF STNSAGFKQN TINVPVGYND PAHVLANQPH MTYRDQHNYP SHQQKQRPFQ NNIVPPELKS RNQRADASPI PQHMVPVKQG VPNLPSNVPL YQQMERMNPN HQHPVNTYKV TQPPYHNNTT NAYGNSRAGN AHMLDGKWSN NPPQMVPKGV RPNQYPQQHV NRYSPQAQPV VPAEYYNGPP PMRAPPMMSH MVPAQEPIRY TAGANRRSFP QGMQQNAYSV PAQPMGAVNS EFYLPEAPQG NKLHGNINKR QERKKLYDNI RSGNFGI //